ID   XYNB_STRSQ              Reviewed;         340 AA.
AC   D7EZJ3;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Endo-1,4-beta-xylanase B;
DE            Short=Xylanase B;
DE            EC=3.2.1.8;
DE   Flags: Precursor;
GN   Name=xynBS9;
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=S9;
RA   Yao G., Li N., Wang Y., Shi P., Chen Q., Yao B.;
RT   "Cloning, expression, and characterization of a xylanase gene, xynBS9, from
RT   Streptomyces sp. S9.";
RL   J. Agric. Sci. Technol. (Beijing) 11:64-70(2009).
CC   -!- FUNCTION: Endo-acting xylanase which specifically cleaves internal
CC       linkages on the xylan backbone, releasing xylooligosaccharides. Is able
CC       to hydrolyze oat spelt xylan and birchwood xylan, releasing xylobiose
CC       and xylotriose as the major products. {ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000269|Ref.1};
CC   -!- ACTIVITY REGULATION: Is inhibited by Ag(+) and Hg(2+) in vitro. EDTA
CC       and other metal cations such as Na(+), K(+), Ca(2+), Cu(2+), Mg(2+),
CC       Fe(3+), and Zn(2+) have no effect on catalytic activity.
CC       {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=3741 umol/min/mg enzyme with oat spelt xylan as substrate (at pH
CC         6.5 and 60 degrees Celsius) {ECO:0000269|Ref.1};
CC         Vmax=2320 umol/min/mg enzyme with birchwood xylan as substrate (at pH
CC         6.5 and 60 degrees Celsius) {ECO:0000269|Ref.1};
CC       pH dependence:
CC         Optimum pH is 6-7. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; EU660499; ACF57947.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7EZJ3; -.
DR   SMR; D7EZJ3; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..52
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..340
FT                   /note="Endo-1,4-beta-xylanase B"
FT                   /id="PRO_0000424417"
FT   DOMAIN          54..239
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   DOMAIN          248..340
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        227
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
SQ   SEQUENCE   340 AA;  36245 MW;  84EBAF44059CCCB3 CRC64;
     MHDAPAQRKR RRPGRIGPLP RSSRFARLKL LIASACAALL ATLALPPGAA HAQTVTSNQT
     GNHNGYFYSF WTDAPGTVSA TMGSGGNYST SWRNTGNFVI GKGWSTGGRR TVTYSGSFNP
     SGNAYLTLYG WSRNPLVEYY IVDNWGTYRP TGTFKGTVTT DGGTYDIYQT TRYNAPSIEG
     NKTFNQYWSV RQQKRTGGTI TTGNHFDAWA RAGMQLGSHD YMIMATEGYQ SSGSSNITVG
     GTSGGGGGGG GGGGCTATLS AGERWDDRYN LNVSVSGSSN WTVTMNVPSP ATILSTWNIT
     ATWPSSQVLV ARPNGSGNNF GVTIKHNGNW TWPTVSCSTG